Characteristics of two types of chloride channel in sarcoplasmic reticulum vesicles from rabbit skeletal muscle

Kourie, Joseph I.; Laver, Derek R.; Junankar, Pauline R.; Gage, Peter W.; Dulhunty, Angela F.

doi:10.1016/s0006-3495(96)79564-4

Cited by 61 publications

(53 citation statements)

References 59 publications

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“…The effect of DIDS was to block any action of GTP and palmitate in promoting Ca 2ϩ uptake. This action of DIDS was half-maximal between 10 and 30 M in preventing both palmitate-and oxalatedependent Ca 2ϩ accumulation in the presence of GTP (data not shown), clearly within the sensitivity range described above for anion channels of the SR and ER (51,52). DIDS had little inhibitory effect on the initial rate of ATP-dependent Ca 2ϩ pumping in the absence of palmitate or oxalate; at longer time intervals, a slight reduction in Ca 2ϩ accumulation may reflect the permissive role of anion channels in mediating charge equilibration and allowing an increase in the equilibrium level of Ca 2ϩ to be attained within the ER.…”

Section: What Is the Process By Which Fatty Acids Mediate Gtp-dependesupporting

confidence: 82%

“…Anion channels in both the SR (45, 47-49) and ER (44, 50) have also been well described. In rabbit SR, there appear to be two different anion channels that are blocked by 8 and 80 M DIDS, respectively (51), and in rat brain ER, anion channels are blocked by DIDS in the 15-100 M range (52). We therefore investigated whether DIDS would modify the action of either palmitate or oxalate in promoting Ca 2ϩ accumulation in the presence of GTP.…”

Section: What Is the Process By Which Fatty Acids Mediate Gtp-dependementioning

confidence: 99%

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Fatty Acid-mediated Calcium Sequestration within Intracellular Calcium Pools

Rys-Sikora

Gill

1998

Journal of Biological Chemistry

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Section: What Is the Process By Which Fatty Acids Mediate Gtp-dependesupporting

confidence: 82%

Section: What Is the Process By Which Fatty Acids Mediate Gtp-dependementioning

confidence: 99%

Fatty Acid-mediated Calcium Sequestration within Intracellular Calcium Pools

Rys-Sikora

Gill

1998

Journal of Biological Chemistry

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“…Modifications in the bilayer thickness, mediated via lipid solvents, e.g., n-decane, contribute to changes in channel gating kinetics of ion channels (31,36) and particularly those formed with short peptides, e.g., the 15-amino acid gramicidin-formed channel (43). Therefore, standardizing the specific membrane capacitance (Cb) and its time independence is important in comparative and detailed investigations of ion channel characteristics.…”

Section: Solutionsmentioning

confidence: 99%

“…The maximal current was also obtained by measuring the distance (in pA) between the peak at 0 pA (representing the closed state) and the extreme peak on the right (representing the open state) in the allpoint histogram generated using CHANNEL 2 (see Ref. 36). Both methods were used, and the results were generally in agreement.…”

Section: Solutionsmentioning

confidence: 99%

“…In this study we have examined the Cu 2ϩ dependency of A␤(1-42)-formed channels. Bilayers were formed across a 150-m hole in the wall of a 1-ml Delrin T cup using a mixture of palmitoyl-oleoyl-phosphatidylethanolamine, palmitoyl-oleoyl-phosphatidylserine, and palmitoyl-oleoyl-phosphatidylcholine (5:3:2, by volume) and palmitoyl-oleoyl-phosphatidylethanolamine, palmitoyl-oleoyl-phosphatidylserine (7:3 by volume) (36,40), obtained in chloroform from Avanti Polar Lipids (Alabaster, AL). The lipid mixture was dried under a stream of N 2 and redissolved in n-decane at a final concentration of 50 mg/ml.…”

mentioning

confidence: 99%

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Cu²⁺-induced modification of the kinetics of Aβ(1-42) channels

Bahadi

Farrelly²,

Kenna³

et al. 2003

American Journal of Physiology-Cell Physiology

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We found that the amyloid ␤ peptide A␤(1-42) is capable of interacting with membrane and forming heterogeneous ion channels in the absence of any added Cu 2ϩ or biological redox agents that have been reported to mediate A␤(1-42) toxicity. binds to the histidine residues located at the mouth of the channel. It is proposed that the Cu 2ϩ -binding site of the A␤(1-42)-formed channels is modulated with Cu 2ϩ in a similar way to those of channels formed with the prion protein fragment PrP(106-126), suggesting a possible common mechanism for Cu 2ϩ modulation of A␤ and PrP channel proteins linked to neurodegenerative diseases. neurodegenerative diseases; transitional metals; ion channel pathologies; membrane injuries; calcium homeostasis ALZHEIMER'S DISEASE (AD) is a neurodegenerative disorder that affects the cognitive function of the brain. Pathological changes in AD are characterized by the formation of amyloid plaques and neurofibrillary tangles as well as extensive neuronal loss. The plaques, which accumulate extracellularly in the brain, are composed of aggregates and cause direct neurotoxic effects and/or increase neuronal vulnerability to excitotoxic insults. The major components of the extracellular neurofibrillar bundles are polymerized amyloid ␤ (A␤) peptides A␤(1-40), A␤(1-42), and A␤(1-43). It has been shown that A␤ familial AD-linked mutations of the amyloid protein precursors presenilin-1 and presenilin-2 increase the concentration of A␤(1-42) (53), which has been shown to be toxic in primary neuronal culture at micromolar concentrations (56). The major mechanisms proposed for A␤-induced cytotoxicity involve the loss of Ca 2ϩ homeostasis (see Refs. 46 and 47) and the generation of reactive oxygen species (see Refs. 9,11,12,and 25). The changes in Ca 2ϩ homeostasis could be the result of 1) alterations in endogenous ion transport systems and 2) formation of heterogeneous ion channels (see Refs. 32,33,and 35). Several laboratories have found that A␤(1-40) and other fragments of amyloid precursor protein that contain A␤ also possess the ability to form ion channels in both artificial and biological membranes. Electrophysiological studies have shown that A␤ fragments, e.g., A␤(25-35), A␤(1-40), and A␤(1-42), elicit cation-selective currents when reconstituted into lipid bilayers (1-4, 23, 24, 30, 35, 37, 41, 55) and in the plasma membrane of neurons (28,29,48) as well as in Xenopus oocytes (21). A␤(1-42) and A␤(1-40) increase Ca 2ϩ uptake in liposomes in a dose-dependent manner (38, 49), and soluble A␤s induce Ca 2ϩ influx in neurons and nonneuronal cells (10,50,51,57).In addition to the A␤ being linked to AD, a role for transition metals has also been recognized. Cu 2ϩ and Zn 2ϩ have been implicated in AD (11,12,42), Parkinson's disease (54), prion protein (PrP) (26), and immunoglobulin light chain amyloidosis (17). The mechanisms underlying the interaction between A␤ and these metals may mediate their role in neurotoxicity. There is also evidence to show that A␤, and also PrP, binds Cu 2ϩ (5, 6) to a si...

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